COMPRESSIBILITY AND VOLUME CHANGES OF LYSOZYME DUE TO INHIBITOR BINDING

The adiabatic compressibility and partial specific volume of hen egg-w hite lysozyme, which were determined by the sound velocity and density measurements at 25 degrees C, decreased by addition of its inhibitors , N-acetyl-D-glucosamine oligomers, in the order of monomer > dimer > trimer. This result demonstrates that the inhibitor binding induces th e atomic packing in the cleft of the active site to diminish the struc tural fluctuation of the protein.